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Mitochondria-Anchored Receptor Atg32 Mediates Degradation of Mitochondria via Selective Autophagy

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1006/bbrc.1995.1636openalex-snapshot
Novel System for Monitoring Autophagy in the Yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/j.abb.2007.03.034openalex-snapshot
Selective degradation of mitochondria by mitophagy
inferredcites →https://doi.org/10.1016/j.bbabio.2008.05.001openalex-snapshot
Mitochondrial fusion, fission and autophagy as a quality control axis: The bioenergetic view
inferredcites →https://doi.org/10.1016/j.bbamcr.2006.08.023openalex-snapshot
Pexophagy: Autophagic degradation of peroxisomes
inferredcites →https://doi.org/10.1016/j.devcel.2007.12.011openalex-snapshot
PpAtg30 Tags Peroxisomes for Turnover by Selective Autophagy
inferredcites →https://doi.org/10.1016/j.febslet.2007.01.096openalex-snapshot
Molecular machinery of autophagosome formation in yeast, Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/s1097-2765(01)00263-5openalex-snapshot
Cvt19 Is a Receptor for the Cytoplasm-to-Vacuole Targeting Pathway
inferredcites →https://doi.org/10.1016/s1534-5807(02)00359-3openalex-snapshot
Studies of Cargo Delivery to the Vacuole Mediated by Autophagosomes in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1016/s1534-5807(02)00373-8openalex-snapshot
Mechanism of Cargo Selection in the Cytoplasm to Vacuole Targeting Pathway
inferredcites →https://doi.org/10.1038/nature06639openalex-snapshot
Autophagy fights disease through cellular self-digestion
inferredcites →https://doi.org/10.1038/nature07006openalex-snapshot
Essential role for Nix in autophagic maturation of erythroid cells
inferredcites →https://doi.org/10.1038/ncb1007-1102openalex-snapshot
Autophagosome formation: core machinery and adaptations
inferredcites →https://doi.org/10.1038/ncb1723openalex-snapshot
Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
inferredcites →https://doi.org/10.1038/nrm2708openalex-snapshot
Dynamics and diversity in autophagy mechanisms: lessons from yeast
inferredcites →https://doi.org/10.1038/sj.cdd.4401697openalex-snapshot
Impairing the bioenergetic status and the biogenesis of mitochondria triggers mitophagy in yeast
inferredcites →https://doi.org/10.1038/sj.cdd.4402167openalex-snapshot
Mdm38 protein depletion causes loss of mitochondrial K+/H+ exchange activity, osmotic swelling and mitophagy
inferredcites →https://doi.org/10.1038/sj.emboj.7601963openalex-snapshot
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
inferredcites →https://doi.org/10.1038/sj.emboj.7601972openalex-snapshot
Quality control of mitochondria: protection against neurodegeneration and ageing
inferredcites →https://doi.org/10.1073/pnas.0708818104openalex-snapshot
NIX is required for programmed mitochondrial clearance during reticulocyte maturation
inferredcites →https://doi.org/10.1074/jbc.m406960200openalex-snapshot
Uth1p Is Involved in the Autophagic Degradation of Mitochondria
inferredcites →https://doi.org/10.1074/jbc.m605940200openalex-snapshot
Aup1p, a Yeast Mitochondrial Protein Phosphatase Homolog, Is Required for Efficient Stationary Phase Mitophagy and Cell Survival
inferredcites →https://doi.org/10.1074/jbc.m702824200openalex-snapshot
p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy
inferredcites →https://doi.org/10.1074/jbc.m802182200openalex-snapshot
Structural Basis for Sorting Mechanism of p62 in Selective Autophagy
inferredcites →https://doi.org/10.1074/jbc.m802403200openalex-snapshot
Mitophagy in Yeast Occurs through a Selective Mechanism
inferredcites →https://doi.org/10.1074/jbc.r500016200openalex-snapshot
Molecular Mechanisms and Regulation of Specific and Nonspecific Autophagy Pathways in Yeast
inferredcites →https://doi.org/10.1083/jcb.119.2.301openalex-snapshot
Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction.
inferredcites →https://doi.org/10.1083/jcb.124.6.903openalex-snapshot
Ultrastructural analysis of the autophagic process in yeast: detection of autophagosomes and their characterization
inferredcites →https://doi.org/10.1083/jcb.141.3.625openalex-snapshot
Peroxisome Degradation by Microautophagy in Pichia pastoris : Identification of Specific Steps and Morphological Intermediates
inferredcites →https://doi.org/10.1083/jcb.147.2.435openalex-snapshot
Formation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast
inferredcites →https://doi.org/10.1083/jcb.150.6.1507openalex-snapshot
Tor-Mediated Induction of Autophagy via an Apg1 Protein Kinase Complex
inferredcites →https://doi.org/10.1083/jcb.153.2.381openalex-snapshot
Cvt9/Gsa9 Functions in Sequestering Selective Cytosolic Cargo Destined for the Vacuole
inferredcites →https://doi.org/10.1083/jcb.200412022openalex-snapshot
Impairment of starvation-induced and constitutive autophagy in Atg7 -deficient mice
inferredcites →https://doi.org/10.1083/jcb.200507002openalex-snapshot
p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
inferredcites →https://doi.org/10.1083/jcb.200809125openalex-snapshot
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
inferredcites →https://doi.org/10.1089/rej.2005.8.3openalex-snapshot
Selective Mitochondrial Autophagy, or Mitophagy, as a Targeted Defense Against Oxidative Stress, Mitochondrial Dysfunction, and Aging
inferredcites →https://doi.org/10.1091/mbc.e04-11-1035openalex-snapshot
Atg11 Links Cargo to the Vesicle-forming Machinery in the Cytoplasm to Vacuole Targeting Pathway
inferredcites →https://doi.org/10.1091/mbc.e06-02-0145openalex-snapshot
The Novel F-Box Protein Mfb1p Regulates Mitochondrial Connectivity and Exhibits Asymmetric Localization in Yeast
inferredcites →https://doi.org/10.1091/mbc.e07-10-1048openalex-snapshot
Organization of the Pre-autophagosomal Structure Responsible for Autophagosome Formation
inferredcites →https://doi.org/10.1093/emboj/20.21.5971openalex-snapshot
The pre‐autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
inferredcites →https://doi.org/10.1093/genetics/144.4.1425openalex-snapshot
Genomic Libraries and a Host Strain Designed for Highly Efficient Two-Hybrid Selection in Yeast
inferredcites →https://doi.org/10.1093/genetics/147.2.435openalex-snapshot
Large Scale Identification of Genes Involved in Cell Surface Biosynthesis and Architecture in Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1101/gad.1599207openalex-snapshot
Autophagy: process and function
inferredcites →https://doi.org/10.1111/j.1365-2443.2008.01238.xopenalex-snapshot
Structural basis of target recognition by Atg8/LC3 during selective autophagy
inferredcites →https://doi.org/10.1152/physiol.00013.2008openalex-snapshot
How to Live Long and Prosper: Autophagy, Mitochondria, and Aging
inferredcites →https://doi.org/10.1242/jcs.111.16.2455openalex-snapshot
Escape of mitochondrial DNA to the nucleus in ymel yeast is mediated by vacuolar-dependent turnover of abnormal mitochondrial compartments
inferredcites →https://doi.org/10.1371/journal.pbio.0040423openalex-snapshot
Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response
inferredcites →https://doi.org/10.4161/auto.4034openalex-snapshot
Selective and Non-Selective Autophagic Degradation of Mitochondria in Yeast
inferredcites →https://doi.org/10.4161/auto.5902openalex-snapshot
The selectivity of autophagy and its role in cell death and survival

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Intricacies of Lipid Supply in Autophagic Membrane Expansion
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Mitochondrial clearance: mechanisms and roles in cellular fitness
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Liquid droplet formation and cytoplasm to vacuole targeting of aminopeptidase I are temperature sensitive in Saccharomyces cerevisiae
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Autophagy in a Nutshell
inferred← citeshttps://doi.org/10.1002/1873-3468.14742openalex-snapshot
Structural view on autophagosome formation
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A brief overview of BNIP3L/NIX receptor‐mediated mitophagy
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Mechanisms and Roles of Mitophagy
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Mitochondria
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THE DYNAMIC CHONDRIOME
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Lysosomes and Mitophagy
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A Get‐Together to Tear It Apart
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The Dynamic Chondriome: Control of Number, Shape, Size and Motility of Mitochondria
inferred← citeshttps://doi.org/10.1002/cbin.11156openalex-snapshot
Vrl1 relies on its VPS9‐domain to play a role in autophagy in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1002/cne.24213openalex-snapshot
Three‐dimensional analysis of somatic mitochondrial dynamics in fission‐deficient injured motor neurons using FIB/SEM
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Mitophagy as a Protective Mechanism against Myocardial Stress
inferred← citeshttps://doi.org/10.1002/embr.201438501openalex-snapshot
ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy
inferred← citeshttps://doi.org/10.1002/iub.1122openalex-snapshot
Mitochondrial protein homeostasis
inferred← citeshttps://doi.org/10.1002/iub.2585openalex-snapshot
Mitophagy in aging and longevity
inferred← citeshttps://doi.org/10.1002/iub.261openalex-snapshot
PGC‐1α activation as a therapeutic approach in mitochondrial disease
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Mitophagy as a Protective Mechanism against Myocardial Stress
inferred← citeshttps://doi.org/10.1002/jcb.24004openalex-snapshot
Control of mitochondrial activity by miRNAs
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Ferritinophagy/ferroptosis: Iron‐related newcomers in human diseases
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The effect of fasting or calorie restriction on mitophagy induction: a literature review
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Deterioration of mitochondrial biogenesis and degradation in the endometrium is a cause of subfertility in cows
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Autophagy: cellular and molecular mechanisms
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Mitochondrial Dysfunction in Age‐Related Metabolic Disorders
inferred← citeshttps://doi.org/10.1002/wrna.1522openalex-snapshot
On the edge of degradation: Autophagy regulation by RNA decay
inferred← citeshttps://doi.org/10.1007/124_2017_6openalex-snapshot
Redox Control of Autophagy in Photosynthetic Organisms
inferred← citeshttps://doi.org/10.1007/7651_2017_11openalex-snapshot
Investigation of Yeast Mitophagy with Fluorescence Microscopy and Western Blotting
inferred← citeshttps://doi.org/10.1007/7651_2017_12openalex-snapshot
MitoPho8Δ60 Assay as a Tool to Quantitatively Measure Mitophagy Activity
inferred← citeshttps://doi.org/10.1007/7651_2017_13openalex-snapshot
Mitophagy in Yeast: A Screen of Mitophagy-Deficient Mutants
inferred← citeshttps://doi.org/10.1007/7651_2017_15openalex-snapshot
Exploring MicroRNAs on NIX-Dependent Mitophagy
inferred← citeshttps://doi.org/10.1007/7651_2017_38openalex-snapshot
Short Overview
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Monitoring of Iron Depletion-Induced Mitophagy in Pathogenic Yeast
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Mitochondrial Dysfunction in Neurodegenerative Disease: Protein Aggregation, Autophagy, and Oxidative Stress
inferred← citeshttps://doi.org/10.1007/978-1-0716-4067-8_1openalex-snapshot
Fluorescence Microscopy and Immunoblotting for Mitophagy in Budding Yeast
inferred← citeshttps://doi.org/10.1007/978-1-4419-7002-2_5openalex-snapshot
Autophagy and Longevity: Lessons from C. elegans
inferred← citeshttps://doi.org/10.1007/978-1-4614-4599-9_11openalex-snapshot
Cell-Death Pathways and Mitochondria
inferred← citeshttps://doi.org/10.1007/978-1-4614-6561-4_1openalex-snapshot
Historical Overview of Autophagy
inferred← citeshttps://doi.org/10.1007/978-1-4939-0799-1_11openalex-snapshot
Assays for Autophagy II: Mitochondrial Autophagy
inferred← citeshttps://doi.org/10.1007/978-1-4939-6824-4_20openalex-snapshot
Assays for Mitophagy in Yeast
inferred← citeshttps://doi.org/10.1007/978-1-4939-8873-0_42openalex-snapshot
Assays to Monitor Mitophagy in Drosophila
inferred← citeshttps://doi.org/10.1007/978-1-4939-8873-0_44openalex-snapshot
Methods for Studying Mitophagy in Yeast
inferred← citeshttps://doi.org/10.1007/978-3-030-05067-2_10openalex-snapshot
Autophagy in Neurodegenerative Diseases
inferred← citeshttps://doi.org/10.1007/978-3-030-58532-7_5openalex-snapshot
Structure and Function of the Mitochondrion
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Mitochondrial Dysfunction and Mitophagy: Physiological Implications in Cardiovascular Health
inferred← citeshttps://doi.org/10.1007/978-3-031-88121-3_4openalex-snapshot
Autophagy Receptors Couple Cargo Destined to Be Degraded with the Core Autophagy Machinery
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Introduction to Autophagy in Physiology and Pathophysiology
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Mitophagy in Starvation
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Mitophagy in Starvation
inferred← citeshttps://doi.org/10.1007/978-3-642-27928-7_6openalex-snapshot
Quality control of proteins and organelles by autophagy
inferred← citeshttps://doi.org/10.1007/978-4-431-55200-0_18openalex-snapshot
Mitosomes in Entamoeba histolytica
inferred← citeshttps://doi.org/10.1007/978-94-007-1291-1_3openalex-snapshot
Mitochondrial Dynamics and Autophagy
inferred← citeshttps://doi.org/10.1007/978-94-007-2561-4openalex-snapshot
Aging Research in Yeast
inferred← citeshttps://doi.org/10.1007/978-94-007-2561-4_11openalex-snapshot
Cellular Homeostasis in Fungi: Impact on the Aging Process
inferred← citeshttps://doi.org/10.1007/978-94-007-2561-4_8openalex-snapshot
Amino Acid Homeostasis and Chronological Longevity in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1007/978-94-007-5724-0_19openalex-snapshot
Autophagy of Chloroplasts During Leaf Senescence
inferred← citeshttps://doi.org/10.1007/978-94-017-8984-4_3openalex-snapshot
Regulation of Mitochondrial Function by MicroRNA
inferred← citeshttps://doi.org/10.1007/978-981-15-0602-4_19openalex-snapshot
Autophagy in Mitochondrial Quality Control
inferred← citeshttps://doi.org/10.1007/978-981-16-2830-6_16openalex-snapshot
Screening for Genes Involved in Autophagy
inferred← citeshttps://doi.org/10.1007/978-981-16-7606-2_5openalex-snapshot
Mitophagy Impairments as Culprit of Alzheimer’s Disease
inferred← citeshttps://doi.org/10.1007/s00018-010-0435-2openalex-snapshot
Mitochondrial dynamics in cell death and neurodegeneration
inferred← citeshttps://doi.org/10.1007/s00018-015-1935-xopenalex-snapshot
Biogenesis of endosome-derived transport carriers
inferred← citeshttps://doi.org/10.1007/s00018-019-03015-6openalex-snapshot
The SEACIT complex is involved in the maintenance of vacuole–mitochondria contact sites and controls mitophagy
inferred← citeshttps://doi.org/10.1007/s00018-019-03246-7openalex-snapshot
Post-translational modification and protein sorting to small extracellular vesicles including exosomes by ubiquitin and UBLs
inferred← citeshttps://doi.org/10.1007/s00109-012-0934-8openalex-snapshot
Etiology of Crohn’s disease: many roads lead to autophagy
inferred← citeshttps://doi.org/10.1007/s00281-010-0219-7openalex-snapshot
Autophagy and lipids: tightening the knot
inferred← citeshttps://doi.org/10.1007/s00294-018-0809-9openalex-snapshot
Heat shock transcriptional factor mediates mitochondrial unfolded protein response
inferred← citeshttps://doi.org/10.1007/s00441-016-2472-0openalex-snapshot
Roles of mitophagy in cellular physiology and development
inferred← citeshttps://doi.org/10.1007/s00441-016-2485-8openalex-snapshot
Mitochondrial quality control by the Pink1/Parkin system
inferred← citeshttps://doi.org/10.1007/s00508-014-0592-7openalex-snapshot
Biological pathways involved in the development of inflammatory bowel disease
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From signal transduction to autophagy of plant cell organelles: lessons from yeast and mammals and plant-specific features
inferred← citeshttps://doi.org/10.1007/s00709-011-0296-zopenalex-snapshot
Variations on a theme: plant autophagy in comparison to yeast and mammals
inferred← citeshttps://doi.org/10.1007/s10522-014-9515-2openalex-snapshot
Mitochondrial function and mitochondrial DNA maintenance with advancing age
inferred← citeshttps://doi.org/10.1007/s10522-018-9779-zopenalex-snapshot
Dual roles of mitochondrial fusion gene FZO1 in yeast age asymmetry and in longevity mediated by a novel ATG32-dependent retrograde response
inferred← citeshttps://doi.org/10.1007/s10539-020-09749-zopenalex-snapshot
Internal perspectivalism: the solution to generality problems about proper function and natural norms
inferred← citeshttps://doi.org/10.1007/s10565-020-09534-4openalex-snapshot
A new sight: topology-dependent mitophagy
inferred← citeshttps://doi.org/10.1007/s11033-019-05218-3openalex-snapshot
Lawsone, a 2-hydroxy-1,4-naphthoquinone from Lawsonia inermis (henna), produces mitochondrial dysfunctions and triggers mitophagy in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1007/s11033-024-10123-5openalex-snapshot
Mechanistic exploration of ubiquitination-mediated pathways in cerebral ischemic injury
inferred← citeshttps://doi.org/10.1007/s11064-013-1033-0openalex-snapshot
Mitophagy in Ischaemia/Reperfusion Induced Cerebral Injury
inferred← citeshttps://doi.org/10.1007/s12640-022-00475-wopenalex-snapshot
The Role of PTEN-L in Modulating PINK1-Parkin-Mediated Mitophagy
inferred← citeshttps://doi.org/10.1007/s13238-011-1104-4openalex-snapshot
Role of plant autophagy in stress response
inferred← citeshttps://doi.org/10.1007/s13238-016-0328-8openalex-snapshot
Structural insights into the recognition of phosphorylated FUNDC1 by LC3B in mitophagy
inferred← citeshttps://doi.org/10.1007/s13340-011-0020-4openalex-snapshot
Roles of autophagy in pancreatic β-cell function and type 2 diabetes
inferred← citeshttps://doi.org/10.1007/s40139-013-0033-8openalex-snapshot
Phosphorylation Events in Selective Mitophagy: Possible Biochemical Markers?
inferred← citeshttps://doi.org/10.1007/s40263-018-0497-5openalex-snapshot
Activating Autophagy as a Therapeutic Strategy for Parkinson’s Disease
inferred← citeshttps://doi.org/10.1007/s44297-023-00002-zopenalex-snapshot
UvSnx4 is required for conidiation, pathogenicity and stress responses by regulating mitophagy and macroautophagy in Ustilaginoidea virens
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00002-xopenalex-snapshot
Molecular Process and Physiological Significance of Mitophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00003-1openalex-snapshot
Principles of Mitophagy and Beyond
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00004-3openalex-snapshot
Quality Control in Mitochondria
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00007-9openalex-snapshot
Role of Nix in the Maturation of Erythroid Cells through Mitochondrial Autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-405528-5.00010-9openalex-snapshot
Atg32 Confers Selective Mitochondrial Sequestration as a Cargo for Autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-405877-4.00004-4openalex-snapshot
Selective Autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-407173-5.00003-0openalex-snapshot
Autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-801032-7.00017-4openalex-snapshot
The Role of Autophagy Receptors in Mitophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-802936-7.00006-4openalex-snapshot
Cargo Proteins Facilitate the Formation of Transport Vesicles, but not Autophagosomes
inferred← citeshttps://doi.org/10.1016/b978-0-12-802937-4.00008-9openalex-snapshot
The Role of Autophagy and Mitophagy in Mitochondrial Diseases
inferred← citeshttps://doi.org/10.1016/b978-0-12-805253-2.00004-3openalex-snapshot
Mechanism and Regulation of Selective Mitophagy in Cardiometabolic Disease
inferred← citeshttps://doi.org/10.1016/b978-0-12-805420-8.00008-1openalex-snapshot
The Role of Atg9 in Yeast Autophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-821562-3.00037-xopenalex-snapshot
Mitochondrial biogenesis and mitophagy
inferred← citeshttps://doi.org/10.1016/b978-0-12-822416-8.00005-1openalex-snapshot
Updates on mitochondria, calorie restriction, and aging
inferred← citeshttps://doi.org/10.1016/b978-0-323-95672-7.00018-2openalex-snapshot
Autophagy and Huntington's disease
inferred← citeshttps://doi.org/10.1016/b978-0-323-98808-7.00007-2openalex-snapshot
Precision mitochondrial medicine: Uncovering pathways across diverse diseases
inferred← citeshttps://doi.org/10.1016/b978-0-443-15260-3.00001-6openalex-snapshot
Formation of mitophagosomes
inferred← citeshttps://doi.org/10.1016/b978-0-443-15260-3.00023-5openalex-snapshot
The Sodom and Gomorrah conundrum of yeast mitophagy
inferred← citeshttps://doi.org/10.1016/b978-0-443-40535-8.00011-9openalex-snapshot
Mitochondrial metabolism and trafficking in cancer
inferred← citeshttps://doi.org/10.1016/bs.ircmb.2016.12.003openalex-snapshot
Molecular Biology Digest of Cell Mitophagy
inferred← citeshttps://doi.org/10.1016/bs.ircmb.2018.05.005openalex-snapshot
Novel Insights Into the Anti-aging Role of Mitophagy
inferred← citeshttps://doi.org/10.1016/bs.ircmb.2020.10.001openalex-snapshot
Autophagic cell death in viral infection: Do TAM receptors play a role?
inferred← citeshttps://doi.org/10.1016/bs.mcb.2019.10.006openalex-snapshot
Detection of mitophagy in mammalian cells, mice, and yeast
inferred← citeshttps://doi.org/10.1016/bs.mcb.2020.10.014openalex-snapshot
Assessing autophagic flux in yeast
inferred← citeshttps://doi.org/10.1016/bs.mie.2016.09.085openalex-snapshot
Monitoring the Formation of Autophagosomal Precursor Structures in Yeast Saccharomyces cerevisiae
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Methods for Studying Interactions Between Atg8/LC3/GABARAP and LIR-Containing Proteins
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The interplay between mitochondrial functionality and genome integrity in the prevention of human neurologic diseases
inferred← citeshttps://doi.org/10.1016/j.actatropica.2015.09.013openalex-snapshot
Identification of TgAtg8–TgAtg3 interaction in Toxoplasma gondii
inferred← citeshttps://doi.org/10.1016/j.arr.2014.12.007openalex-snapshot
Mitochondria to nucleus signaling and the role of ceramide in its integration into the suite of cell quality control processes during aging
inferred← citeshttps://doi.org/10.1016/j.arr.2023.101955openalex-snapshot
Mitochondrial dysfunction in aging
inferred← citeshttps://doi.org/10.1016/j.bbabio.2013.11.009openalex-snapshot
Roles of autophagy in chloroplast recycling
inferred← citeshttps://doi.org/10.1016/j.bbabio.2015.04.010openalex-snapshot
Mitochondria, autophagy and age-associated neurodegenerative diseases: New insights into a complex interplay
inferred← citeshttps://doi.org/10.1016/j.bbabio.2020.148302openalex-snapshot
The regulation of mitochondrial homeostasis by the ubiquitin proteasome system
inferred← citeshttps://doi.org/10.1016/j.bbadis.2013.11.024openalex-snapshot
In vivo functions of Drp1: Lessons learned from yeast genetics and mouse knockouts
inferred← citeshttps://doi.org/10.1016/j.bbagen.2011.08.001openalex-snapshot
Mitochondria and autophagy: Critical interplay between the two homeostats
inferred← citeshttps://doi.org/10.1016/j.bbagen.2013.09.002openalex-snapshot
MicroRNAs as regulators of mitochondrial function: Role in cancer suppression
inferred← citeshttps://doi.org/10.1016/j.bbagen.2021.129858openalex-snapshot
Regulatory mechanisms of mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbagen.2021.129916openalex-snapshot
Mitophagy in plants
inferred← citeshttps://doi.org/10.1016/j.bbagen.2021.129932openalex-snapshot
Yeast mitophagy: Unanswered questions
inferred← citeshttps://doi.org/10.1016/j.bbagen.2022.130203openalex-snapshot
An overview of the molecular mechanisms of mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbalip.2016.02.001openalex-snapshot
Lipid transfer and metabolism across the endolysosomal–mitochondrial boundary
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2010.08.007openalex-snapshot
Mitophagy and Parkinson's disease: The PINK1–parkin link
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2011.07.011openalex-snapshot
Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.02.010openalex-snapshot
The retrograde response: When mitochondrial quality control is not enough
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.02.012openalex-snapshot
Mitochondrial morphology in mitophagy and macroautophagy
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.05.024openalex-snapshot
Staying cool in difficult times: Mitochondrial dynamics, quality control and the stress response
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.06.025openalex-snapshot
Proteolytic control of mitochondrial function and morphogenesis
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2012.08.007openalex-snapshot
Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.03.019openalex-snapshot
Substrate recognition in selective autophagy and the ubiquitin–proteasome system
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.06.031openalex-snapshot
Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2014.12.039openalex-snapshot
Ceramide induced mitophagy and tumor suppression
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.01.005openalex-snapshot
Mitophagy in yeast: Molecular mechanisms and physiological role
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.02.022openalex-snapshot
Mitochondrial autophagy: Origins, significance, and role of BNIP3 and NIX
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.02.024openalex-snapshot
Mitophagy and mitochondrial dynamics in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.03.013openalex-snapshot
Selective removal of mitochondria via mitophagy: distinct pathways for different mitochondrial stresses
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.05.010openalex-snapshot
Mitochondrial degradation and energy metabolism
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.09.032openalex-snapshot
Peroxisome homeostasis: Mechanisms of division and selective degradation of peroxisomes in mammals
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2015.12.022openalex-snapshot
Regulation of peroxisome dynamics by phosphorylation
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2017.04.012openalex-snapshot
Mitochatting – If only we could be a fly on the cell wall
inferred← citeshttps://doi.org/10.1016/j.bbapap.2011.05.013openalex-snapshot
Proteases in autophagy
inferred← citeshttps://doi.org/10.1016/j.bbrc.2010.02.106openalex-snapshot
Programmed cell clearance: Molecular regulation of the elimination of apoptotic cell corpses and its role in the resolution of inflammation
inferred← citeshttps://doi.org/10.1016/j.bbrc.2016.12.112openalex-snapshot
Induction of autophagy by phosphate starvation in an Atg11-dependent manner in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/j.bbrc.2017.12.163openalex-snapshot
The Nem1-Spo7 protein phosphatase complex is required for efficient mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbrc.2018.04.114openalex-snapshot
The ER membrane insertase Get1/2 is required for efficient mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbrc.2018.05.123openalex-snapshot
The TORC1 signaling pathway regulates respiration-induced mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbrc.2018.10.034openalex-snapshot
A novel role for Bcl2l13 in promoting beige adipocyte biogenesis
inferred← citeshttps://doi.org/10.1016/j.bbrc.2022.10.052openalex-snapshot
The Dep1 protein: A new regulator of mitophagy in yeast
inferred← citeshttps://doi.org/10.1016/j.bbrc.2025.152254openalex-snapshot
Mitophagy: A double-edged sword in tumor cell death regulation and therapeutic response
inferred← citeshttps://doi.org/10.1016/j.biocel.2011.06.002openalex-snapshot
Ubiquitin-dependent mitochondrial protein degradation
inferred← citeshttps://doi.org/10.1016/j.biocel.2012.07.006openalex-snapshot
Mitophagy: A process that adapts to the cell physiology
inferred← citeshttps://doi.org/10.1016/j.biocel.2014.05.010openalex-snapshot
Mitophagy mechanisms and role in human diseases
inferred← citeshttps://doi.org/10.1016/j.blre.2017.04.001openalex-snapshot
Autophagy: A necessary event during erythropoiesis
inferred← citeshttps://doi.org/10.1016/j.cca.2020.02.024openalex-snapshot
Bnip3 in mitophagy: Novel insights and potential therapeutic target for diseases of secondary mitochondrial dysfunction
inferred← citeshttps://doi.org/10.1016/j.ceb.2009.12.002openalex-snapshot
Cytoprotective roles for autophagy
inferred← citeshttps://doi.org/10.1016/j.ceb.2009.12.004openalex-snapshot
The role of the Atg1/ULK1 complex in autophagy regulation
inferred← citeshttps://doi.org/10.1016/j.ceb.2009.12.009openalex-snapshot
Autophagy in infection
inferred← citeshttps://doi.org/10.1016/j.ceb.2011.03.003openalex-snapshot
Ubiquitination-mediated autophagy against invading bacteria
inferred← citeshttps://doi.org/10.1016/j.cellsig.2018.04.002openalex-snapshot
S6 kinase 1 plays a key role in mitochondrial morphology and cellular energy flow
inferred← citeshttps://doi.org/10.1016/j.celrep.2015.01.044openalex-snapshot
Synthetic Quantitative Array Technology Identifies the Ubp3-Bre5 Deubiquitinase Complex as a Negative Regulator of Mitophagy
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.03.127openalex-snapshot
Mitophagy Directs Muscle-Adipose Crosstalk to Alleviate Dietary Obesity
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.05.064openalex-snapshot
The PP2A-like Protein Phosphatase Ppg1 and the Far Complex Cooperatively Counteract CK2-Mediated Phosphorylation of Atg32 to Inhibit Mitophagy
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.12.050openalex-snapshot
A Mammalian Mitophagy Receptor, Bcl2-L-13, Recruits the ULK1 Complex to Induce Mitophagy
inferred← citeshttps://doi.org/10.1016/j.celrep.2020.107902openalex-snapshot
Mitochondria Associated Degradation Pathway (MAD) Function Beyond the Outer Membrane
inferred← citeshttps://doi.org/10.1016/j.celrep.2023.113051openalex-snapshot
Autophagy-mediated surveillance of Rim4-mRNA interaction safeguards programmed meiotic translation
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.115001openalex-snapshot
AMPK regulates Bcl2-L-13-mediated mitophagy induction for cardioprotection
inferred← citeshttps://doi.org/10.1016/j.celrep.2025.116585openalex-snapshot
Bulk and selective autophagy cooperate to remodel a fungal proteome in response to changing nutrient availability
inferred← citeshttps://doi.org/10.1016/j.chemphyslip.2018.11.001openalex-snapshot
Membrane-binding domains in autophagy
inferred← citeshttps://doi.org/10.1016/j.chom.2014.03.012openalex-snapshot
Self and Nonself: How Autophagy Targets Mitochondria and Bacteria
inferred← citeshttps://doi.org/10.1016/j.cmet.2011.04.008openalex-snapshot
High-Mobility Group Box 1 Is Essential for Mitochondrial Quality Control
inferred← citeshttps://doi.org/10.1016/j.conb.2011.10.016openalex-snapshot
Mitochondrial dynamics and mitophagy in Parkinson's disease: disordered cellular power plant becomes a big deal in a major movement disorder
inferred← citeshttps://doi.org/10.1016/j.crvi.2012.04.004openalex-snapshot
L’autophagie chez les plantes : mécanismes, régulations et fonctions
inferred← citeshttps://doi.org/10.1016/j.cub.2018.01.004openalex-snapshot
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
inferred← citeshttps://doi.org/10.1016/j.cub.2022.11.002openalex-snapshot
Orchestration of selective autophagy by cargo receptors
inferred← citeshttps://doi.org/10.1016/j.devcel.2009.07.003openalex-snapshot
A Receptor for Eating Mitochondria
inferred← citeshttps://doi.org/10.1016/j.devcel.2010.07.005openalex-snapshot
The Autophagy Connection
inferred← citeshttps://doi.org/10.1016/j.devcel.2011.06.023openalex-snapshot
Selective Autophagy Regulates Insertional Mutagenesis by the Ty1 Retrotransposon in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.1016/j.devcel.2013.05.024openalex-snapshot
The Scaffold Protein Atg11 Recruits Fission Machinery to Drive Selective Mitochondria Degradation by Autophagy
inferred← citeshttps://doi.org/10.1016/j.devcel.2014.01.012openalex-snapshot
Mitochondrial ER Contacts Are Crucial for Mitophagy in Yeast
inferred← citeshttps://doi.org/10.1016/j.devcel.2014.06.013openalex-snapshot
TRIM Proteins Regulate Autophagy and Can Target Autophagic Substrates by Direct Recognition
inferred← citeshttps://doi.org/10.1016/j.devcel.2017.02.016openalex-snapshot
Cleaning House: Selective Autophagy of Organelles
inferred← citeshttps://doi.org/10.1016/j.devcel.2018.07.011openalex-snapshot
Essential Function of Mec1, the Budding Yeast ATM/ATR Checkpoint-Response Kinase, in Protein Homeostasis
inferred← citeshttps://doi.org/10.1016/j.devcel.2019.06.016openalex-snapshot
Selective Autophagy of Mitochondria on a Ubiquitin-Endoplasmic-Reticulum Platform
inferred← citeshttps://doi.org/10.1016/j.devcel.2021.02.009openalex-snapshot
Quality control of the mitochondrion
inferred← citeshttps://doi.org/10.1016/j.devcel.2024.02.002openalex-snapshot
Rim aperture of yeast autophagic membranes balances cargo inclusion with vesicle maturation
inferred← citeshttps://doi.org/10.1016/j.drup.2024.101170openalex-snapshot
Autophagy in cancer development, immune evasion, and drug resistance
inferred← citeshttps://doi.org/10.1016/j.ecoenv.2020.110667openalex-snapshot
Methylmercury disrupts autophagic flux by inhibiting autophagosome-lysosome fusion in mouse germ cells
inferred← citeshttps://doi.org/10.1016/j.ejmech.2023.116117openalex-snapshot
Targeting autophagy drug discovery: Targets, indications and development trends
inferred← citeshttps://doi.org/10.1016/j.ejps.2019.04.011openalex-snapshot
Autophagy as a molecular target for cancer treatment
inferred← citeshttps://doi.org/10.1016/j.exger.2014.02.015openalex-snapshot
The interplay between mitochondria and autophagy and its role in the aging process
inferred← citeshttps://doi.org/10.1016/j.febslet.2009.12.037openalex-snapshot
Autophagy in the fission yeast Schizosaccharomyces pombe
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.01.007openalex-snapshot
Autophagy in plants and phytopathogens
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.01.018openalex-snapshot
Atg8‐family interacting motif crucial for selective autophagy
inferred← citeshttps://doi.org/10.1016/j.febslet.2010.01.019openalex-snapshot
Molecular mechanism and physiological role of pexophagy
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